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REFINED STRUCTURE OF GLUTATHIONE REDUCTASE AT 1.54 ANGSTROMS RESOLUTION
3GRS
ENTRY 3GRS SUPERSEDES 2GRS
Primary Citation

Refined structure of glutathione reductase at 1.54 A resolution.

Karplus, P.A.,  Schulz, G.E.

Journal: (1987) J.Mol.Biol. 195: 701-729

PubMed: 3656429  
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PubMed Abstract:
The crystal structure of human glutathione reductase has been established at 1.54 A resolution using a restrained least-squares refinement method. Based on 77,690 independent reflections of better than 10 A resolution, a final R-factor of 18.6% was obtained with a... [ Read More & Search PubMed Abstracts ]
 
  •   Molecular Description Hide
    Classification: Oxidoreductase (flavoenzyme)
    Structure Weight: 52517.33
    Molecule: GLUTATHIONE REDUCTASE
    Polymer: 1 Type: protein Length: 478
    Chains: A
    EC#: 1.8.1.7   
    Organism Homo sapiens
    Gene Names GSR GLUR GRD1
    UniProtKB:   Protein Feature View | Search PDB | P00390  
    P00390Molec. ProcessingMitochonGlutathione reductase, mitochondrialMotifFE.C.1.8.1.7: Glutathione-disulfide reductaseUP SitesUniProtKBSCOP domainsFAD/NAD(P)-binding domainFAD/NAD(P)-binFAD/NAD(P)-binding domainFAD/NAD-linked reducta PDB SitesSecstruc3GRS.APDBTooltip
     
  •   Structure Validation Hide

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  •   Related Citations in PDB Entry (REMARK 1) Hide
    Inhibition of Human Glutathione Reductase by the Nitrosourea Drugs 1,3-Bis(2-Chloroethyl)-1-Nitrosurea and 1-(2-Chloroethyl)-3-(2-Hydroxyethyl)-1-Nitrosourea
    Karplus, P.A., Krauth-Siegel, R.L., Schirmer, R.H., Schulz, G.E.
    (1988) Eur.J.Biochem. 171: 193

    Interaction of a Glutathione S-Conjugate with Glutathione Reductase. Kinetic and X-Ray Crystallographic Studies
    Bilzer, M., Krauth-Siegel, R.L., Schirmer, R.H., Akerboom, T.P.M., Sies, H., Schulz, G.E.
    (1984) Eur.J.Biochem. 138: 373

    Comparison of the Three-Dimensional Protein and Nucleotide Structure of the Fad-Binding Domain of P-Hydroxybenzoate Hydroxylase with the Fad-as Well as Nadph-Binding Domains of Glutathione Reductase
    Wierenga, R.K., Drenth, J., Schulz, G.E.
    (1983) J.Mol.Biol. 167: 725

    The Catalytic Mechanism of Glutathione Reductase as Derived from X-Ray Diffraction Analyses of Reaction Intermediates
    Pai, E.F., Schulz, G.E.
    (1983) J.Biol.Chem. 258: 1752

    Fad-Binding Site of Glutathione Reductase
    Schulz, G.E., Schirmer, R.H., Pai, E.F.
    (1982) J.Mol.Biol. 160: 287

    Glutathione Reductase from Human Erythrocytes. The Sequences of the Nadph Domain and of the Interface Domain
    Krauth-Siegel, R.L., Blatterspiel, R., Saleh, M., Schiltz, E., Schirmer, R.H., Untucht-Grau, R.
    (1982) Eur.J.Biochem. 121: 259

    Three-Dimensional Structure of Glutathione Reductase at 2 Angstroms Resolution
    Thieme, R., Pai, E.F., Schirmer, R.H., Schulz, G.E.
    (1981) J.Mol.Biol. 152: 763

    Gene Duplication in Glutathione Reductase
    Schulz, G.E.
    (1980) J.Mol.Biol. 138: 335

    The C-Terminal Fragment of Human Glutathione Reductase Contains the Postulated Catalytic Histidine
    Untucht-Grau, R., Schulz, G.E., Schirmer, R.H.
    (1979) FEBS Lett. 105: 244

    The Structure of the Flavoenzyme Glutathione Reductase
    Schulz, G.E., Schirmer, R.H., Sachsenheimer, W., Pai, E.F.
    (1978) Nature 273: 120

    Low Resolution Structure of Human Erythrocyte Glutathione Reductase
    Zappe, H.A., Krohne-Ehrich, G., Schulz, G.E.
    (1977) J.Mol.Biol. 113: 141

    Crystals of Human Erythrocyte Glutathione Reductase
    Schulz, G.E., Zappe, H., Worthington, D.J., Rosemeyer, M.A.
    (1975) FEBS Lett. 54: 86

     
  •   Source Hide
    Polymer: 1
    Scientific Name: Homo sapiens   Taxonomy   Common Name: Human  
     
  •   Ligand Chemical Component Hide
    Identifier Formula Name View Interactions
    FAD
    Search 
    Download      		FAD C27 H33 N9 O15 P2
    FLAVIN-ADENINE DINUCLEOTIDE
    		FAD:3GRS
    PO4
    Search 
    Download      		PO4 O4 P
    PHOSPHATE ION
     
  •   External Domain Annotations Hide
     
  •   Structural Biology Knowledgebase Data Hide

    Information from the Structural Biology Knowledgebase  

     
 
Data in orange boxes are gathered from external resources (when available).
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  Biological Assembly       
Symmetry: C2 view
Stoichiometry: Homo 2-mer - A2
Biological assembly 1 assigned by authors and generated by PISA,PQS (software)
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  •   Deposition Summary Hide
    Authors:   Schulz, G.E.,  Karplus, P.A.

    Deposition:   1988-02-05
    Release:   1988-04-16
    Last Modified (REVDAT):   2011-07-13

    Previous versions:  1GRS 2GRS
     
  •   Revision History    Hide
    Mouse over text for details
    2011-07-13
    Version format compliance
    2011-07-13
    Biological assembly
     
  •   Experimental Details Hide
    Method:   X-RAY DIFFRACTION
    Exp. Data:
    N/A
    Resolution[Å]:   1.54
    R-Value: 0.186 (work)
    R-Free: n/a
    Space Group: B 2
    Unit Cell:
      Length [Å] Angles [°]
    a = 119.80 α = 90.00 
    b = 84.50 β = 90.00 
    c = 63.20 γ = 58.70 
     
Biological Assembly Image for 3GRS
REFINED STRUCTURE OF GLUTATHIONE REDUCTASE AT 1.54 ANGSTROMS RESOLUTION
Protein chains are colored from the N-terminal to the C-terminal using a rainbow (spectral) color gradient

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